Intra‐ and intermolecular interactions of the catalytic domains of human CD45 protein tyrosine phosphatase

FEBS Letters

Moriyama, Yoshinori²  Noumi, Takato³  Hayami-Noumi, Keiko¹  Tsuchiya, Tomofusa¹ 

[1] Department of Microbiology, Faculty of Pharmaceutical Sciences, Okayama University, 3-1-1 Tsushima-naka, Okayama 700-8530, Japan;Department of Neuronal Cell Biology, Faculty of Pharmaceutical Sciences, Okayama University, 3-1-1 Tsushima-naka, Okayama 700-8530, Japan;Department of Molecular Biology, Tsukuba Research Laboratories, Glaxo Wellcome K.K. 43 Wadai, Tsukuba, Ibaraki 300-4247, Japan

关键词: CD45;    Protein tyrosine phosphatase;    Protein-protein interaction;    Two-hybrid system;    PTP;    protein tyrosine phosphatase;    PCR;    polymerase chain reaction;    3-AT;    3-amino-1;    2;    4-triazole;    ONPG;    o-nitrophenyl β-D-galactopyranoside;    CPRG;    chlorophenolred-β-D-galactopyranoside;    TCR;    T-cell antigen receptor complex;    EGF-R;    epidermal growth factor receptor;   

DOI  :  10.1016/S0014-5793(00)01200-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have investigated protein-protein interaction between distinct domains of the human CD45 cytoplasmic region using a yeast two-hybrid system. Consequently, we have found that the spacer region between two tandem PTP domains specifically interacts with the membrane-distal PTP domain (D2). This interaction is mediated by a stretch of amino acid residues in the carboxyl-terminal half of the spacer region. Although the membrane proximal region does not directly interact with either of the two PTP domains, it appears to function in stabilizing the interaction between the spacer region and D2. We also demonstrate that the interaction between the spacer region and D2 might take place intramolecularly.

【 授权许可】

Unknown